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Dimerization of lipocalin allergens.

Niemi MH, Rytkönen-Nissinen M, Miettinen I, Jänis J, Virtanen T, Rouvinen J - Sci Rep (2015)

Bottom Line: We have determined two different dimeric crystal structures for bovine dander lipocalin Bos d 2, which was earlier described as a monomeric allergen.The crystal structure analysis of all other determined lipocalin allergens also revealed oligomeric structures which broadly utilize inherent structural features of the β-sheet in dimer formation.According to the moderate size of monomer-monomer interfaces, most of these dimers would be transient in solution.

View Article: PubMed Central - PubMed

Affiliation: Department of Chemistry and Biocenter Kuopio, University of Eastern Finland, PO BOX 111, 80101 Joensuu, Finland.

ABSTRACT
Lipocalins are one of the most important groups of inhalant animal allergens. The analysis of structural features of these proteins is important to get insights into their allergenicity. We have determined two different dimeric crystal structures for bovine dander lipocalin Bos d 2, which was earlier described as a monomeric allergen. The crystal structure analysis of all other determined lipocalin allergens also revealed oligomeric structures which broadly utilize inherent structural features of the β-sheet in dimer formation. According to the moderate size of monomer-monomer interfaces, most of these dimers would be transient in solution. Native mass spectrometry was employed to characterize quantitatively transient dimerization of two lipocalin allergens, Bos d 2 and Bos d 5, in solution.

No MeSH data available.


The oligomeric structures for 10 lipocalin allergens observed in crystals.One monomer is in green, other monomers in grey. The structural elements forming monomer-monomer interfaces are labelled.
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f3: The oligomeric structures for 10 lipocalin allergens observed in crystals.One monomer is in green, other monomers in grey. The structural elements forming monomer-monomer interfaces are labelled.

Mentions: Rat n 1 allergen is a major urinary protein of male rats. The tetrameric structure of Rat n 1 has been reported in monoclinic and orthorhombic crystal forms89. The structure contains a complete tetramer with 222 symmetry, each monomer packs against two other monomers having two different interfaces. The larger monomer-monomer interface (708 Å2) is formed by strand D-F and especially by the L4 loop between β-strands D and E (Fig. 3a). Three aromatic hydrophobic residues Tyr72, Phe81, and Phe108 can be found on the interface, which suggests strong hydrophobic interactions, which would favour oligomer formation. The second interface is smaller (457 Å2) and formed mainly by a β-strand C. Tyr86 from this β-strand packs with the same residue from the second monomer. Because the second interface is smaller with fewer hydrophobic interactions, this would indicate that tetramer dissociates easily to dimers at lower protein concentrations.


Dimerization of lipocalin allergens.

Niemi MH, Rytkönen-Nissinen M, Miettinen I, Jänis J, Virtanen T, Rouvinen J - Sci Rep (2015)

The oligomeric structures for 10 lipocalin allergens observed in crystals.One monomer is in green, other monomers in grey. The structural elements forming monomer-monomer interfaces are labelled.
© Copyright Policy - open-access
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC4561914&req=5

f3: The oligomeric structures for 10 lipocalin allergens observed in crystals.One monomer is in green, other monomers in grey. The structural elements forming monomer-monomer interfaces are labelled.
Mentions: Rat n 1 allergen is a major urinary protein of male rats. The tetrameric structure of Rat n 1 has been reported in monoclinic and orthorhombic crystal forms89. The structure contains a complete tetramer with 222 symmetry, each monomer packs against two other monomers having two different interfaces. The larger monomer-monomer interface (708 Å2) is formed by strand D-F and especially by the L4 loop between β-strands D and E (Fig. 3a). Three aromatic hydrophobic residues Tyr72, Phe81, and Phe108 can be found on the interface, which suggests strong hydrophobic interactions, which would favour oligomer formation. The second interface is smaller (457 Å2) and formed mainly by a β-strand C. Tyr86 from this β-strand packs with the same residue from the second monomer. Because the second interface is smaller with fewer hydrophobic interactions, this would indicate that tetramer dissociates easily to dimers at lower protein concentrations.

Bottom Line: We have determined two different dimeric crystal structures for bovine dander lipocalin Bos d 2, which was earlier described as a monomeric allergen.The crystal structure analysis of all other determined lipocalin allergens also revealed oligomeric structures which broadly utilize inherent structural features of the β-sheet in dimer formation.According to the moderate size of monomer-monomer interfaces, most of these dimers would be transient in solution.

View Article: PubMed Central - PubMed

Affiliation: Department of Chemistry and Biocenter Kuopio, University of Eastern Finland, PO BOX 111, 80101 Joensuu, Finland.

ABSTRACT
Lipocalins are one of the most important groups of inhalant animal allergens. The analysis of structural features of these proteins is important to get insights into their allergenicity. We have determined two different dimeric crystal structures for bovine dander lipocalin Bos d 2, which was earlier described as a monomeric allergen. The crystal structure analysis of all other determined lipocalin allergens also revealed oligomeric structures which broadly utilize inherent structural features of the β-sheet in dimer formation. According to the moderate size of monomer-monomer interfaces, most of these dimers would be transient in solution. Native mass spectrometry was employed to characterize quantitatively transient dimerization of two lipocalin allergens, Bos d 2 and Bos d 5, in solution.

No MeSH data available.